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Humoral factors produced by PBMCs upon stimulation with Lactobacillus delbrueckii ssp. bulgaricus OLL1073R-1-derived exopolysaccharides inhibit HCoV-229E and SARS-CoV-2 replication

ABSTRACT: The COVID-19 pandemic entered a controllable phase due to vaccine and drug development. The development of defense strategies of enhancing host innate immunity remains imperative to counter the emergence of infectious SARS-CoV-2 variants. In this study, we examined the inhibitory effects of Lactobacillus delbrueckii ssp. bulgaricus OLL1073R-1 (OLL1073R-1)-derived exopolysaccharides (R-1 EPS), a natural immunomodulator, against coronaviral infection. The inhibitory effect of R-1 EPS on HCoV-229E was evaluated first and subsequently extended to SARS-CoV-2. Cell culture supernatant was obtained by stimulating human peripheral blood mononuclear cells with R-1 EPS (R-1 sup), and the inhibitory effect of R-1 sup on coronaviruses was evaluated using the human lung cell line, MRC5. High levels of proinflammatory cytokines were detected in R-1 sup, and replication of both HCoV-229E and SARS-CoV-2 was significantly suppressed in MRC5 cells pretreated with R-1 sup. Transcriptomic analysis revealed that type I IFN signaling was upregulated in R-1 sup-treated MRC5 cells. Our results suggest that humoral factors, including proinflammatory cytokines, in R-1 sup, enhance type I IFN response, resulting in a broad spectral inhibitory effect on coronaviruses. This study provides a scientific basis for the application of OLL1073R-1 and R-1 EPS as preventive strategies against SARS-CoV-2 and other coronaviruses.

ORGANISM(S): Homo sapiens

PROVIDER: GSE295798 | GEO | 2025/08/30

REPOSITORIES: GEO

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Project description:Human coronaviruses have become an increasing threat to global health; three highly pathogenic strains have emerged since the early 2000s, including most recently SARS-CoV-2, the cause of COVID-19. A better understanding of the molecular mechanisms of coronavirus pathogenesis is needed, including how these highly virulent strains differ from those that cause milder, common-cold like disease. While significant progress has been made in understanding how SARS-CoV-2 proteins interact with the host cell, non-structural protein 3 (nsp3) has largely been omitted from the analyses. Nsp3 is a viral protease with important roles in viral protein biogenesis, replication complex formation, and modulation of host ubiquitinylation and ISGylation. Herein, we use affinity purification-mass spectrometry to study the host-viral protein-protein interactome of nsp3 from five coronavirus strains: pathogenic strains SARS-CoV-2, SARS-CoV, and MERS-CoV, and endemic common-cold strains hCoV-229E and hCoV-OC43. We divide each nsp3 into three fragments and use tandem mass tag technology to directly compare the interactors across the five strains for each fragment. We find that that few interactors are common across all variants for a particular fragment, but we identify shared patterns between select variants, such as ribosomal proteins enriched in the N-terminal fragment (nsp3.1) analysis for SARS-CoV-2 and SARS-CoV. We also identify unique biological processes enriched for individual homologs, for instance nuclear protein important for the middle fragment of hCoV-229E, as well as ribosome biogenesis of the MERS nsp3.1 homolog. Lastly, we further investigate the interaction of the SARS-CoV-2 nsp3.1 N-terminal fragment with ATF6, a regulator of the unfolded protein response. We show that SARS-CoV-2 nsp3.1 directly binds to ATF6 and can suppress the ATF6 stress response. Characterizing the host interactions of nsp3 widens our understanding of how coronaviruses co-opt cellular pathways and presents new avenues for host-targeted antiviral therapeutics.

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Humoral factors produced by PBMCs upon stimulation with Lactobacillus delbrueckii ssp. bulgaricus OLL1073R-1-derived exopolysaccharides inhibit HCoV-229E and SARS-CoV-2 replication

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